Q63TV1 (PYRD_BURPS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotate dehydrogenase (quinone)
EC=1.3.5.2

Alternative name(s):
DHOdehase
Short name=DHOD
Short name=DHODase
Dihydroorotate oxidase

Gene names

Name:	pyrD
Ordered Locus Names:	BPSL1866

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei)

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP MF_00225
Catalytic activity	(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP MF_00225
Cofactor	Binds 1 FMN per subunit By similarity. HAMAP MF_00225
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP MF_00225
Subunit structure	Monomer By similarity. HAMAP MF_00225
Subcellular location	Cell membrane; Peripheral membrane protein By similarity HAMAP MF_00225.
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cell membrane Membrane
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro UMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 342	342	Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225		PRO_0000148429
Regions
	Nucleotide binding	65 – 69	5	FMN By similarity
	Nucleotide binding	321 – 322	2	FMN By similarity
	Region	114 – 118	5	Substrate binding By similarity
	Region	249 – 250	2	Substrate binding By similarity
Sites
	Active site	178	1	Nucleophile By similarity
	Binding site	69	1	Substrate By similarity
	Binding site	89	1	FMN; via amide nitrogen By similarity
	Binding site	142	1	FMN By similarity
	Binding site	175	1	FMN By similarity
	Binding site	175	1	Substrate By similarity
	Binding site	180	1	Substrate By similarity
	Binding site	220	1	FMN By similarity
	Binding site	248	1	FMN; via carbonyl oxygen By similarity
	Binding site	271	1	FMN; via amide nitrogen By similarity
	Binding site	300	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63TV1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 796E35619C05A53C	FASTA	342	36,323
	10 20 30 40 50 60 MFSSLYPLAR ASLFKMDAED AHHLTLRMLG AAGRTGLACA LSPRVPDAPR TVMGLSFRNP 70 80 90 100 110 120 VGLAAGLDKD GAAIDGFAAL GFGFIEVGTV TPRAQPGNPR PRMFRLPEAD AIINRMGFNN 130 140 150 160 170 180 SGVDQFVKNV QAARYRGVLG LNIGKNADTP IERAADDYLY CLERVYPFAS YVTINISSPN 190 200 210 220 230 240 TKNLRQLQGA GELDALLAAL KDKQRRLADL HGKLVPLALK IAPDLDDEQV KEIAATLLRH 250 260 270 280 290 300 DIEGVIATNT TLSREAVKGL PHADEAGGLS GRPVFDASNA VIRKLRAELG DAVPIIGVGG 310 320 330 340 IFSGEDARAK LAAGAALVQL YTGFIYRGPA LVAECVKAIA RG

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571965 Genomic DNA. Translation: CAH35865.1.
RefSeq	YP_108465.1. NC_006350.1.
3D structure databases
ProteinModelPortal	Q63TV1.
SMR	Q63TV1. Positions 5-339.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3093839.
GenomeReviews	Gene locus BPSL1866 in contig BX571965_GR.
KEGG	bps:BPSL1866.
PATRIC	19263765. VBIBurPse99623_2102.
Phylogenomic databases
HOGENOM	HBG351027.
OMA	SYVTVNI.
PhylomeDB	Q63TV1.
ProtClustDB	PRK05286.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL1866-MONOMER.
Family and domain databases
HAMAP	MF_00225. DHO_dh_type2. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005719. Dihydroorotate_DH_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K00226.
Pfam	PF01180. DHO_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMs	TIGR01036. PyrD_sub2. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRD_BURPS

Accession

Primary (citable) accession number: Q63TV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program